Development of a computational tool for high throughput protein structure determination using NMR residential dipolar coupling restraints is proposed. NMR residual dipolar couplings, which provide long-range orientation information of protein structures, are much easier to obtain experimentally than other structural information. This long-range orientation ordering information is proposed to be used as a complementary to our refined force field, which by itself can describe a protein structure to certain accuracy. The native structure of a protein is identified through an efficient conformational search using the self-guided molecular dynamics simulation method. The incorporation of NMR residual dipolar coupling information into the force field will help the protein folding simulation converge to the native structure, enhance the accuracy of simulation result, and make the native structure distinguishable from other low energy structures. We expect this development will provide a more expedient and less expensive method for protein structure determination than current NMR methods, and achieve high throughout protein structure determination. PROPOSED COMMERCIAL APPLICATION: NOT AVAILABLE